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Database: UniProt
Entry: A0A0B5HPG9_9ACTN
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ID   A0A0B5HPG9_9ACTN        Unreviewed;       291 AA.
AC   A0A0B5HPG9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Undecaprenyl-diphosphatase {ECO:0000256|ARBA:ARBA00021581, ECO:0000256|HAMAP-Rule:MF_01006};
DE            EC=3.6.1.27 {ECO:0000256|ARBA:ARBA00012374, ECO:0000256|HAMAP-Rule:MF_01006};
DE   AltName: Full=Bacitracin resistance protein {ECO:0000256|ARBA:ARBA00032932, ECO:0000256|HAMAP-Rule:MF_01006};
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000256|ARBA:ARBA00032707, ECO:0000256|HAMAP-Rule:MF_01006};
GN   Name=uppP {ECO:0000256|HAMAP-Rule:MF_01006};
GN   ORFNames=SVTN_05850 {ECO:0000313|EMBL:AJF64010.1};
OS   Streptomyces vietnamensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=362257 {ECO:0000313|EMBL:AJF64010.1, ECO:0000313|Proteomes:UP000031774};
RN   [1] {ECO:0000313|EMBL:AJF64010.1, ECO:0000313|Proteomes:UP000031774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GIMV4.0001 {ECO:0000313|Proteomes:UP000031774};
RA   Deng M.R., Guo J., Ma L.Y., Feng G.D., Mo C.Y., Zhu H.H.;
RT   "Complete genome sequence of Streptomyces vietnamensis strain GIMV4.0001, a
RT   genetic manipulable producer of the benzoisochromanequinone antibiotic
RT   granaticin.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate
CC       (UPP). Confers resistance to bacitracin. {ECO:0000256|HAMAP-
CC       Rule:MF_01006}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-
CC         trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:28094, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58405, ChEBI:CHEBI:60392; EC=3.6.1.27;
CC         Evidence={ECO:0000256|ARBA:ARBA00000759, ECO:0000256|HAMAP-
CC         Rule:MF_01006};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01006};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01006}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- MISCELLANEOUS: Bacitracin is thought to be involved in the inhibition
CC       of peptidoglycan synthesis by sequestering undecaprenyl diphosphate,
CC       thereby reducing the pool of lipid carrier available.
CC       {ECO:0000256|HAMAP-Rule:MF_01006}.
CC   -!- SIMILARITY: Belongs to the UppP family. {ECO:0000256|ARBA:ARBA00010621,
CC       ECO:0000256|HAMAP-Rule:MF_01006}.
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DR   EMBL; CP010407; AJF64010.1; -; Genomic_DNA.
DR   RefSeq; WP_041128094.1; NZ_CP010407.1.
DR   AlphaFoldDB; A0A0B5HPG9; -.
DR   STRING; 362257.SVTN_05850; -.
DR   KEGG; svt:SVTN_05850; -.
DR   HOGENOM; CLU_060296_1_0_11; -.
DR   Proteomes; UP000031774; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01006; Undec_diphosphatase; 1.
DR   InterPro; IPR003824; UppP.
DR   NCBIfam; TIGR00753; undec_PP_bacA; 1.
DR   PANTHER; PTHR30622; UNDECAPRENYL-DIPHOSPHATASE; 1.
DR   PANTHER; PTHR30622:SF4; UNDECAPRENYL-DIPHOSPHATASE; 1.
DR   Pfam; PF02673; BacA; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251, ECO:0000256|HAMAP-
KW   Rule:MF_01006};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01006}; Cell shape {ECO:0000256|HAMAP-Rule:MF_01006};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01006};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01006};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01006};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031774};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01006};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01006}.
FT   TRANSMEM        87..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        198..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        228..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT   TRANSMEM        263..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
SQ   SEQUENCE   291 AA;  30997 MW;  747292566CA24AA0 CRC64;
     MSWFESFILG LVQGLTEFLP ISSSAHLRLT AAFAGWEDPG AAFTAITQIG TETAVLIYFR
     KDIARIVSAW FRSLTNKAMR SDHDAQMGWL VIVGSIPIGV LGVTLKDQIE GPFRDLRLTA
     TTLIVMGVVL GIADRLAARD EAGGRHRAAR ERKTLKDLGV RDGLIYGVCQ AMALIPGVSR
     SGATISGGLL MGYTREAAAR YSFLLAIPAV LASGGMELKD AAADGGVSWG PTIFATIVAF
     AVGYAVIAWF MKFITTKSFM PFVIYRIALG ILLIVLVAMG VLSPHAGESA G
//
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